The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

Qing Li; Jianxun Qi; Wei Zhang; Christopher J Vavricka; Yi Shi; Jinhua Wei; Enguang Feng; Jingshan Shen; Jilong Chen; Di Liu; Jianhua He; Jinghua Yan; Hong Liu; Hualiang Jiang; Maikun Teng; Xuebing Li; George F Gao

doi:10.1038/nsmb.1909

The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site

Nat Struct Mol Biol. 2010 Oct;17(10):1266-8. doi: 10.1038/nsmb.1909. Epub 2010 Sep 19.

Authors

Qing Li¹, Jianxun Qi, Wei Zhang, Christopher J Vavricka, Yi Shi, Jinhua Wei, Enguang Feng, Jingshan Shen, Jilong Chen, Di Liu, Jianhua He, Jinghua Yan, Hong Liu, Hualiang Jiang, Maikun Teng, Xuebing Li, George F Gao

Affiliation

¹ CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.

PMID: 20852645
DOI: 10.1038/nsmb.1909

Abstract

Influenza A virus neuraminidase can be classified into groups 1 and 2 on the basis of its primary structure. The main structural feature of group 1 neuraminidase is an extra cavity in the active site, the 150-cavity. Here we present the crystal structure of neuraminidase from the 2009 pandemic H1N1 influenza strain. In contrast to other characterized N1 neuraminidases, which are all members of group 1, 2009 H1N1 neuraminidase does not have a 150-cavity.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Catalytic Domain
Crystallography, X-Ray
Influenza A Virus, H1N1 Subtype / enzymology*
Influenza A Virus, H1N1 Subtype / genetics
Models, Molecular
Molecular Sequence Data
N-Acetylneuraminic Acid / metabolism
Neuraminidase / chemistry*
Neuraminidase / classification
Neuraminidase / genetics
Protein Conformation
Sequence Alignment
Sequence Homology, Amino Acid

Substances

Neuraminidase
N-Acetylneuraminic Acid

Associated data

PDB/3NSS